In this study, the binding mechanism between bovine serum albumin (BSA) and three gingerols ([6]-, [8]- and [10]-gingerol) was evaluated to explore an effective strategy for improving solubility and stability of gingerols. The fluorescence analysis suggested gingerols could bind with BSA to form a stable BSA/gingerols complex and [10]-gingerol had the strongest binding affinity (K_a = 4.016 × 10⁴ L/mol) at 298 K. Thermodynamic parameters and molecular modeling validated that hydrophobic interaction and hydrogen bonds were the main driving force for the interaction of BSA/gingerols. Gingerols bound to BSA at site I (subdomain IIA) resulted in a conformational change of BSA with a structure shrinkage, which was responsible for the decrease of surface hydrophobicity. The formation of BSA/gingerols complexes promoted the solubility of [6]-, [8]- and [10]-gingerol increasing by 1.50, 6.04 and 23.50 times, respectively. In addition, the stability and antioxidant capacity of gingerols was significantly improved after binding with BSA.

本研究评估了牛血清白蛋白 (BSA) 与三种姜辣素（[6]-、[8]- 和 [10]-姜辣素）之间的结合机制，以探索提高姜辣素溶解度和稳定性的有效策略。荧光分析表明姜酚可以与 BSA 结合形成稳定的 BSA/姜酚复合物，[10]-姜酚具有最强的结合亲和力（K _a  = 4.016 × 10 ⁴L/mol) 在 298 K。热力学参数和分子模型验证了疏水相互作用和氢键是 BSA/姜醇相互作用的主要驱动力。在位点 I（子域 IIA）与 BSA 结合的姜酚导致 BSA 的构象变化和结构收缩，这是表面疏水性降低的原因。BSA/姜酚复合物的形成促进了[6]-、[8]-和[10]-姜酚的溶解度分别增加了1.50、6.04和23.50倍。此外，姜辣素与BSA结合后，其稳定性和抗氧化能力得到显着提高。